ID NUOG_RICCN Reviewed; 671 AA. AC Q92G92; DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot. DT 15-MAY-2007, sequence version 2. DT 27-MAR-2024, entry version 125. DE RecName: Full=NADH-quinone oxidoreductase subunit G; DE EC=7.1.1.-; DE AltName: Full=NADH dehydrogenase I subunit G; DE AltName: Full=NDH-1 subunit G; GN Name=nuoG; OrderedLocusNames=RC1231; OS Rickettsia conorii (strain ATCC VR-613 / Malish 7). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales; OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group. OX NCBI_TaxID=272944; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC VR-613 / Malish 7; RX PubMed=11557893; DOI=10.1126/science.1061471; RA Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V., RA Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.; RT "Mechanisms of evolution in Rickettsia conorii and R. prowazekii."; RL Science 293:2093-2098(2001). CC -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur CC (Fe-S) centers, to quinones in the respiratory chain. Couples the redox CC reaction to proton translocation (for every two electrons transferred, CC four hydrogen ions are translocated across the cytoplasmic membrane), CC and thus conserves the redox energy in a proton gradient (By CC similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + CC NAD(+); Xref=Rhea:RHEA:57888, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646, CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124; CC -!- COFACTOR: CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000250}; CC Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000250}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250}; CC Note=Binds 2 [4Fe-4S] clusters per subunit. {ECO:0000250}; CC -!- SIMILARITY: Belongs to the complex I 75 kDa subunit family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAL03769.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE006914; AAL03769.1; ALT_INIT; Genomic_DNA. DR PIR; G97853; G97853. DR RefSeq; WP_041471777.1; NC_003103.1. DR AlphaFoldDB; Q92G92; -. DR SMR; Q92G92; -. DR GeneID; 928385; -. DR KEGG; rco:RC1231; -. DR PATRIC; fig|272944.4.peg.1411; -. DR HOGENOM; CLU_000422_11_6_5; -. DR Proteomes; UP000000816; Chromosome. DR GO; GO:0016020; C:membrane; IEA:InterPro. DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro. DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW. DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro. DR CDD; cd00207; fer2; 1. DR CDD; cd02773; MopB_Res-Cmplx1_Nad11; 1. DR Gene3D; 3.10.20.740; -; 1. DR Gene3D; 3.30.70.20; -; 1. DR Gene3D; 3.40.50.740; -; 2. DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1. DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf. DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type. DR InterPro; IPR006656; Mopterin_OxRdtase. DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom. DR InterPro; IPR000283; NADH_UbQ_OxRdtase_75kDa_su_CS. DR InterPro; IPR010228; NADH_UbQ_OxRdtase_Gsu. DR InterPro; IPR019574; NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd. DR InterPro; IPR015405; NDUFS1-like_C. DR NCBIfam; TIGR01973; NuoG; 1. DR PANTHER; PTHR43105:SF13; NADH-UBIQUINONE OXIDOREDUCTASE 75 KDA SUBUNIT, MITOCHONDRIAL; 1. DR PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1. DR Pfam; PF13510; Fer2_4; 1. DR Pfam; PF00384; Molybdopterin; 1. DR Pfam; PF10588; NADH-G_4Fe-4S_3; 1. DR Pfam; PF09326; NADH_dhqG_C; 1. DR SMART; SM00929; NADH-G_4Fe-4S_3; 1. DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1. DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1. DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1. DR PROSITE; PS51085; 2FE2S_FER_2; 1. DR PROSITE; PS51839; 4FE4S_HC3; 1. DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1. DR PROSITE; PS00641; COMPLEX1_75K_1; 1. DR PROSITE; PS00642; COMPLEX1_75K_2; 1. DR PROSITE; PS00643; COMPLEX1_75K_3; 1. PE 3: Inferred from homology; KW 2Fe-2S; 4Fe-4S; Iron; Iron-sulfur; Metal-binding; NAD; Quinone; KW Translocase. FT CHAIN 1..671 FT /note="NADH-quinone oxidoreductase subunit G" FT /id="PRO_0000118561" FT DOMAIN 1..78 FT /note="2Fe-2S ferredoxin-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465" FT DOMAIN 78..117 FT /note="4Fe-4S His(Cys)3-ligated-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01184" FT DOMAIN 215..271 FT /note="4Fe-4S Mo/W bis-MGD-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004" FT BINDING 34 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000250" FT BINDING 45 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000250" FT BINDING 48 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000250" FT BINDING 62 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000250" FT BINDING 94 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01184" FT BINDING 98 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01184" FT BINDING 101 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01184" FT BINDING 107 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01184" FT BINDING 146 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 149 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 152 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 196 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="2" FT /evidence="ECO:0000250" SQ SEQUENCE 671 AA; 74809 MW; 9D9BB900EE9AE68D CRC64; MIKLNVDGSE IEVSEGSTVY QACTQAGKEI PHFCYHQRLK IAGNCRMCLV EMEKSPKPIA SCAMPVSNGM VIHTDTPMVK KAREGVMEFL LINHPLDCPI CDQGGECNLQ DQAFRYGKGT NRFHENKRSI KDKYMGPLIK TAMTRCIQCT RCIRFASDIA GIEEIGAIHR GEHIEVTSYL EQTLDSEISG NMIDICPVGA LNSKPYAFKA RKWELKHTAS IGVHDAEGSN IRIDSRGDEV MRILPRVNEE INEEWLSDKN RFSYDGLKYQ RLDRPYIRKN GKLVEASWSE ALKTVADKIK SVKPEKIVAI AGSLSSVEAM FMLKTLLQKL GSNNYSVNQF DYKLDTMQRG NYLFNTTIAG IEKADLCLLI GANPRQIAPV LNSRIGMRVR ADSLKVARIG GGHNQTYKIQ DLGSDIKIIE ELAIGTHEFT KALKAAKYLM IIVGDGVYAR DDGYAILSLI HKIVTEYNIM RDDWKGFNIL HNHASIVGGL DIGFNTPIKL EELELAYLLG TDAIPFDKLK STFIIYQGHH GDAGASSADV ILPAAAYTEQ SGIYVNLEGR PQIAEKAVSP VGVAKEDIEI IKELAGYLKI DIGMDNLQEV RVRLAKEYKV FASIDRIIEN KFSKFSSKDK LSKEPITAEP INYYMTDVIS KNSVTMAKCV EAKEARDEEV A //